ID A0A0P9ITY8_RHOGW Unreviewed; 386 AA.
AC A0A0P9ITY8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Cystathionine gamma-synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=RHOBADRAFT_66877 {ECO:0000313|EMBL:KPV72890.1};
OS Rhodotorula graminis (strain WP1).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV72890.1, ECO:0000313|Proteomes:UP000053890};
RN [1] {ECO:0000313|EMBL:KPV72890.1, ECO:0000313|Proteomes:UP000053890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP1 {ECO:0000313|EMBL:KPV72890.1,
RC ECO:0000313|Proteomes:UP000053890};
RX PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT graminis WP1.";
RL Front. Microbiol. 6:978-978(2015).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|RuleBase:RU362118}.
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DR EMBL; KQ474085; KPV72890.1; -; Genomic_DNA.
DR RefSeq; XP_018268939.1; XM_018419109.1.
DR AlphaFoldDB; A0A0P9ITY8; -.
DR STRING; 578459.A0A0P9ITY8; -.
DR GeneID; 28979555; -.
DR OMA; DWTKQLF; -.
DR OrthoDB; 5482552at2759; -.
DR Proteomes; UP000053890; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808:SF35; CYSTATHIONINE GAMMA-SYNTHASE (AFU_ORTHOLOGUE AFUA_7G01590); 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000053890}.
FT REGION 34..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 207
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 386 AA; 42633 MW; CB568AD6037FB59F CRC64;
MAPLQRTAFA TRAIHQDSEL SGAEVAASLS LSTTFRHPDP EVDGVEPGYD DEWDPSRPSR
DVYSRETKPT TTRAEHVLSS IIGQPTILFP SGMAAFWAIL LHVRPDIIAI TGGYGGCHEA
IKIYRRTKGE DQVQLIQLDD EYPHGKKLLV WVETPLNPLG TSRSLDKYAK RAHAAGGILG
VDSTFGPPPM QDPFKWGVDI VMHSGTKYLN GHSDLLAGTV SVRDKADWLK LWNDRTFTGA
NIGSLDVWLL LRSLRTLDVR VKRQSKTATR LAQWLATQVG GGVVDKVYHT SLQDNADELL
GPGKQMELGP ACFSVVLKSK DMASRLPNKL KLFIHATSLG GVESLIEHRI ISDPSENPCL
VRLSIGLEDF DDLKDDWEHA MQAVRQ
//
